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(3R)-linalyl diphosphate + H2O
? + diphosphate
Substrates: -
Products: -
?
(3S)-linalyl diphosphate + H2O
? + diphosphate
Substrates: -
Products: -
?
geranyl diphosphate
1,8-cineole + diphosphate
geranyl diphosphate + H2O
1,8-cineole + diphosphate
neryl diphosphate + H2O
1,8-cineole + diphosphate
Substrates: -
Products: 61% 1,8-cineole plus 18.5% sabinene, 8% alpha-phellandrene, 3.3% limonene, and 5.5% alpha-terpineol
?
neryl diphosphate + H2O
? + diphosphate
Substrates: -
Products: -
?
additional information
?
-
geranyl diphosphate
1,8-cineole + diphosphate
-
Substrates: -
Products: -
?
geranyl diphosphate
1,8-cineole + diphosphate
Substrates: -
Products: -
?
geranyl diphosphate + H2O
1,8-cineole + diphosphate
Substrates: -
Products: 52% 1,8-cineole plus 0.6% (+)-alpha-thujene, 1.9% (2)-(1S)-alpha-pinene, 14.5% (-)-sabinene, 7.8% (2)-(1S)-beta-pinene, 13.3% myrcene, 4.0% (2)-(4S)-limonene, (E)-2.7% beta-ocimene, 0.8% terpinolene, and 2.4% alpha-terpineol
?
geranyl diphosphate + H2O
1,8-cineole + diphosphate
Substrates: -
Products: -
?
geranyl diphosphate + H2O
1,8-cineole + diphosphate
-
Substrates: -
Products: -
?
geranyl diphosphate + H2O
1,8-cineole + diphosphate
Substrates: -
Products: -
?
geranyl diphosphate + H2O
1,8-cineole + diphosphate
Substrates: -
Products: 80% 1,8-cineole plus 7.9% sabinene, 6.6% alpha-phellandrene, 2.3% limonene, and 1.7% alpha-terpineol
?
geranyl diphosphate + H2O
1,8-cineole + diphosphate
Substrates: -
Products: products are sabinene, beta-myrcene, limonene, 1,8-cineole, and 41% alpha-terpineol
?
geranyl diphosphate + H2O
1,8-cineole + diphosphate
Substrates: -
Products: products are alpha-pinene, beta-pinene, sabinene, beta-myrcene, limonene, 1,8-cineole and alpha-terpineol. 1,8-Cineole and alpha-terpineol are the major products, enzyme synthesizes 2- to 3fold more cineol than alpha-terpineol
?
geranyl diphosphate + H2O
1,8-cineole + diphosphate
Substrates: -
Products: -
?
geranyl diphosphate + H2O
1,8-cineole + diphosphate
Substrates: -
Products: products are alpha-pinene, beta-pinene, sabinene, beta-myrcene, limonene, 1,8-cineole and alpha-terpineol. 1,8-Cineole and alpha-terpineol are the major products, enzyme synthesizes 2- to 3fold more cineol than alpha-terpineol
?
geranyl diphosphate + H2O
1,8-cineole + diphosphate
Substrates: the enzyme releases alpha-terpineol as the main compound as a terpineol synthase (TER). The S to R ratio is 7.9:1 and 7.7:1 in two experimental passages
Products: -
?
geranyl diphosphate + H2O
1,8-cineole + diphosphate
Substrates: -
Products: products are sabinene, beta-myrcene, limonene, 1,8-cineole, and 36% alpha-terpineol
?
geranyl diphosphate + H2O
1,8-cineole + diphosphate
Substrates: -
Products: products are alpha-pinene, beta-pinene, sabinene, beta-myrcene, limonene, 1,8-cineole and alpha-terpineol. 1,8-Cineole and alpha-terpineol are the major products, enzyme synthesizes 2- to 3fold more cineol than alpha-terpineol
?
geranyl diphosphate + H2O
1,8-cineole + diphosphate
Substrates: -
Products: products are alpha-pinene, beta-pinene, sabinene, beta-myrcene, limonene, 1,8-cineole and alpha-terpineol. 1,8-cineole is the major compound comprising ca. 50% of the products. alpha-Terpineol contributes approximately 25%
?
geranyl diphosphate + H2O
1,8-cineole + diphosphate
Substrates: -
Products: -
?
geranyl diphosphate + H2O
1,8-cineole + diphosphate
Substrates: -
Products: major product is 1,8-cineole plus limonene, sabinene, E-beta-ocimene, b-myrcene, alpha-pinene, and alpha-terpineole
?
geranyl diphosphate + H2O
1,8-cineole + diphosphate
Substrates: the enzyme releases alpha-terpineol as the main compound as a terpineol synthase (TER). The S to R ratio is 6.6:1 and 6.5:1 in two experimental passages
Products: -
?
geranyl diphosphate + H2O
1,8-cineole + diphosphate
Substrates: -
Products: 72.4% 1,8-cineole, 7.1% alpha-terpineol, 9.1% beta-pinene, 4.6% alpha-pinene, 3.6% sabinene, 2.2% myrcene, and <1% limonene
?
geranyl diphosphate + H2O
1,8-cineole + diphosphate
Substrates: -
Products: 79% 1,8-cineole plus 20% of a mixture of (+)- and (-)-alpha-pinene, (+)- and (-)-beta-pinene, myrcene and (+)-sabinene
?
geranyl diphosphate + H2O
1,8-cineole + diphosphate
Substrates: -
Products: water is the sole source of the ether oxygen atom of 1,8-cineole
?
geranyl diphosphate + H2O
1,8-cineole + diphosphate
Substrates: -
Products: 1,8-cineole is the single major product
?
geranyl diphosphate + H2O
1,8-cineole + diphosphate
Substrates: -
Products: 1,8-cineole is the single major product
?
additional information
?
-
Substrates: no substrate: farnesyl diphosphate
Products: -
?
additional information
?
-
Substrates: no substrate: farnesyl diphosphate
Products: -
?
additional information
?
-
Substrates: enzyme AaTPS6 produces multiple products with 1,8-cineole as major product (59.28% of total),in addition to ten other products including sabinene and beta-phellandrene (together 19.04%), alpha-terpineol (7.84%), trans-sabinene hydrate(4.03%), (-)-alpha-pinene (3.00%), cis-beta-terpineol (2.51%), beta-myrcene (2.01%), alpha-thujene (0.69%), as well as two unidentified minor products. No activity with farnesyl diphosphate or geranylgeranyl diphosphate
Products: -
?
additional information
?
-
-
Substrates: enzyme AaTPS6 produces multiple products with 1,8-cineole as major product (59.28% of total),in addition to ten other products including sabinene and beta-phellandrene (together 19.04%), alpha-terpineol (7.84%), trans-sabinene hydrate(4.03%), (-)-alpha-pinene (3.00%), cis-beta-terpineol (2.51%), beta-myrcene (2.01%), alpha-thujene (0.69%), as well as two unidentified minor products. No activity with farnesyl diphosphate or geranylgeranyl diphosphate
Products: -
?
additional information
?
-
-
Substrates: no substrate: farnesyl diphosphate
Products: -
?
additional information
?
-
Substrates: with geranyl pyrophosphate (GPP) as a substrate, LnTPS1 catalyzes the formation of mostly 1,8-cineole, with alpha-thujene, alpha-pinene, beta-pinene, alpha-terpinene, gamma-terpinene, alpha-terpinolene, and a few other monoterpenes also produced, as detected by GC-MS analysis
Products: -
?
additional information
?
-
Substrates: enzyme is a multi product enzyme synthesizing simultaneously the seven monoterpenes of the cineole cassette
Products: -
?
additional information
?
-
Substrates: enzyme is a multi product enzyme synthesizing simultaneously the seven monoterpenes of the cineole cassette
Products: -
?
additional information
?
-
Substrates: the formation of alpha-terpineol starts by a nucleophilic attack of water. During this attack, the alpha-terpinyl cation is stabilized by Pi-stacking with a tryptophan side chain (Tryp253). The hypothesized catalytic mechanism of alpha-terpineol-to-1,8-cineole conversion is initiated by a catalytic dyad (His502 and Glu249), acting as a base, and a threonine (Thr278) providing the subsequent rearrangement from terpineol to cineol by catalyzing the autoprotonation of (2S)-2-alpha-terpineol, which is the favored enantiomer product of the recombinant enzymes. Product analysis and quantification by GC-MS. Binding structure of the reactive intermediate alpha-terpinyl cation in the active site of cineole synthase involving residues Trp253, His502, and Thr278, overview. The hydroxyl group of Tyr496 is necessary to control the orientation of Asn419. This Asn itself is proposed to be involved in binding and fixation of the diphosphate moiety of the substrate. Major role of Thr278 in the formation of cineole by fixing the intermediate alpha-terpineol and supporting the autoprotonation of its double bond. Residue Phe266 is relevant for the product outcome of the 1,8-cineole synthase
Products: -
?
additional information
?
-
Substrates: enzyme is a multi product enzyme synthesizing simultaneously the seven monoterpenes of the cineole cassette
Products: -
?
additional information
?
-
Substrates: enzyme is a multi product enzyme synthesizing simultaneously the seven monoterpenes of the cineole cassette
Products: -
?
additional information
?
-
Substrates: the formation of alpha-terpineol strats by a nucleophilic attack of water. During this attack, the alpha-terpinyl cation is stabilized by Pi-stacking with a tryptophan side chain (Tryp253). The hypothesized catalytic mechanism of alpha-terpineol-to-1,8-cineole conversion is initiated by a catalytic dyad (His502 and Glu249), acting as a base, and a threonine (Thr278) providing the subsequent rearrangement from terpineol to cineol by catalyzing the autoprotonation of (2S)-2-alpha-terpineol, which is the favored enantiomer product of the recombinant enzymes. Product analysis and quantification by GC-MS
Products: -
?
additional information
?
-
Substrates: no substrate: farnesyl diphosphate
Products: -
?
additional information
?
-
Substrates: no substrate: farnesyl diphosphate
Products: -
?
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evolution
enzyme AaTPS6 belongs to the terpene synthases family, TPS-b subfamily
evolution
the amounts and ratios of alpha-terpineol enantiomers is species-specific for cineole synthases and terpineol synthases of different species, overview. For Nicotinana forgetiana, the S:R ratio ((S)-(-)-alpha-terpineol to (R)-(+)-alpha-terpineol) is 7.7-7.9:1
evolution
the monoterpene synthase belongs to the terpene synthases superfamily, TPS-b clade
metabolism
cyclization reactions of monoterpene synthases, overview. Substrate GPP is ionized by diphosphate elimination, resulting in the geranyl cation. Subsequently, this cation is converted into the linalyl cation and alpha-terpinyl cation. The synthesis of the acyclic beta-myrcene might proceed via the geranyl cation or via the linalyl cation by deprotonation. The intermediate alpha-terpinyl cation is the precursor for all cyclic monoterpenes. The 2,7-ring closure results in the pinyl cation, which is deprotonated to synthesize beta-pinene and alpha-pinene. Sabinene, with a cyclopropane ring, is released after two carbocation formations and 2,6-ring closure. alpha-Terpineol is formed after water capture of the alpha-terpinyl cation. Broken lines indicate possible reactions leading to 1,8-cineole. A cyclization reaction resulting in 1,8-cineole uses alpha-terpineol as a precursor. Enzyme structure homology modelling
metabolism
cyclization reactions of monoterpene synthases, overview. Substrate GPP is ionized by diphosphate elimination, resulting in the geranyl cation. Subsequently, this cation is converted into the linalyl cation and alpha-terpinyl cation. The synthesis of the acyclic beta-myrcene might proceed via the geranyl cation or via the linalyl cation by deprotonation. The intermediate alpha-terpinyl cation is the precursor for all cyclic monoterpenes. The 2,7-ring closure results in the pinyl cation, which is deprotonated to synthesize beta-pinene and alpha-pinene. Sabinene, with a cyclopropane ring, is released after two carbocation formations and 2,6-ring closure. alpha-Terpineol is formed after water capture of the alpha-terpinyl cation. Broken lines indicate possible reactions leading to 1,8-cineole. A cyclization reaction resulting in 1,8-cineole uses alpha-terpineol as a precursor. Enzyme structure homology modelling
metabolism
in Artemisia annua, three monoterpene synthases AaTPS2, AaTPS5, and AaTPS6, produce beta-myrcene, camphene, and 1,8-cineole as the major products, respectively
physiological function
fresh Laurus nobilis leaves, the monoterpene 1,8-cineole is the main volatile compound, and alpha-terpinyl acetate, terpinene-4-ol, alpha- and beta-pinene, sabinene, and linalool are reported to occur in appreciable levels. The 1,8-cineole content is also higher in femal flowers, overview
physiological function
the monoterpene synthase TPS6 might play a role in plant-environment interactions
additional information
the amino acids at positions 147, 148, and 266 determine the different terpineol-cineole ratios in Nicotiana suaveolens cineole synthase and Nicotiana langsdorffii terpineol synthase
additional information
the amino acids at positions 147, 148, and 266 determine the different terpineol-cineole ratios in Nicotiana suaveolens cineole synthase and Nicotiana langsdorffii terpineol synthase. Homology modeling of 1,8-cineole synthases of Nicotiana forgetiana and Nicotiana suaveolens
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N419A
site-directed mutagenesis, the mutation results in a drastic drop of enzyme activity, and except for traces of alpha-terpineol, no cyclic products are detected
T278A
site-directed mutagenesis, the product composition of the Thr mutant is altered compared to the wild-type enzyme, the most striking change is the decreased amount of 1,8-cineole. Thus, this mutation converts the wild-type cineole synthase into an alpha-terpineol synthase. Assuming that alpha-terpineol is a distinct precursor in the biosynthesis of 1,8-cineole, a decrease of cineole within the product profile indicates a disturbed reaction mechanism of the cyclization of alpha-terpineol toward 1,8-cineole
T279A
site-directed mutagenesis, the mutation of this residue does not change the product composition but leads to an overall increase of activity in Nicotiana forgetiana
W253A
site-directed mutagenesis, the mutant reveals a strongly decreased amount of cyclic monoterpenes
W253M
site-directed mutagenesis, an exchange to Met does not seem to provide a comparable stabilization
Y496F
site-directed mutagenesis, mutation of the catalytic Tyr causes a drastic decrease of cyclic products
F266C
site-directed mutagenesis, the mutation only slightly alters the product spectrum of the mutant enzyme compared to wild-type enzyme
F266S
site-directed mutagenesis, the mutation shifts the the product spectrum significantly toward alpha-terpineol compared to wild-type enzyme
F266T
site-directed mutagenesis, the mutation only slightly alters the product spectrum of the mutant enzyme compared to wild-type enzyme
F266V
site-directed mutagenesis, the mutation only slightly alters the product spectrum of the mutant enzyme compared to wild-type enzyme
F266Y
site-directed mutagenesis, the mutation only slightly alters the product spectrum of the mutant enzyme compared to wild-type enzyme
N338A
products are 11.7% alpha-pinene, 33.1% sabinene, 33.2% beta-pinene, 16.9% myrcene, 5.1% limonene
N338C
products are 16.1% alpha-pinene, 41% sabinene, 32.1% beta-pinene, 4.7% myrcene, 6.1% limonene
N338I
products are 6.5% alpha-pinene, 48.3% sabinene, 8.2% myrcene, 37% limonene
N338I/A339T
products are 5.4% alpha-pinene, 62.1% sabinene, 6.4% myrcene, 26.1% limonene
N338I/A339T/G447S
products are 5.7% alpha-pinene, 59.6% sabinene, 5.0% myrcene, 29.7% limonene
N338I/A339T/G447S/I449P/P450T
products are 86.8% sabinene, 5.5% myrcene, 7.7% limonene
N338L
products are 4.7% alpha-pinene, 5.6% sabinene, 13.2% beta-pinene, 27.2% myrcene, 49.3% limonene
N338S
products are 9.8% alpha-pinene, 34.5% sabinene, 34.2% beta-pinene, 6.8% myrcene, 2.6% limonene, 5.6% alpha-cineole, 6.5% alpha-terpineol
N338V
products are 61.2% sabinene, 8.0% myrcene, 30.8% limonene
additional information
the N-terminal signal peptide of AaTPS6 (46 amino acid residues) before RR motif is truncated and recombinantly expressed in Escherichia coli strain BL21(DE3)
additional information
-
the N-terminal signal peptide of AaTPS6 (46 amino acid residues) before RR motif is truncated and recombinantly expressed in Escherichia coli strain BL21(DE3)
additional information
although the distributions of the five detectable products sabinene, beta-myrcene, limonene, 1,8-cineole, and alpha-terpineol change slightly in all these mutants compared to wild-type, none of them shifts the product spectrum significantly toward alpha-terpineol, with exception of mutant F266S, overview
additional information
conversion of CinS1 to a sabinene synthase based on an amino acid comparison of the enzyme with Salvia officinalis SabS1 and Salvia pomifera SabS1
additional information
-
conversion of CinS1 to a sabinene synthase based on an amino acid comparison of the enzyme with Salvia officinalis SabS1 and Salvia pomifera SabS1
additional information
exchange of sequences corresponding by homology to the C-terminal domain including the domain spanning alpha-helix, between sabinene synthase and both bornyl diphosphate synthase and cineole synthase. Exchange of residues 304-377 from cineole synthase into sabinene synthase is sufficient to impart the alternative termination chemistry involving water capture to alpha-terpineol and cyclization to 1,8-cineole
additional information
-
exchange of sequences corresponding by homology to the C-terminal domain including the domain spanning alpha-helix, between sabinene synthase and both bornyl diphosphate synthase and cineole synthase. Exchange of residues 304-377 from cineole synthase into sabinene synthase is sufficient to impart the alternative termination chemistry involving water capture to alpha-terpineol and cyclization to 1,8-cineole
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Wise, M.L.; Savage, T.J.; Katahira, E.; Croteau, R.
Monoterpene synthases from common sage (Salvia officinalis). cDNA isolation, characterization, and functional expression of (+)-sabinene synthase, 1,8-cineole synthase, and (+)-bornyl diphosphate synthase
J. Biol. Chem.
273
14891-14899
1998
Salvia officinalis (O81191)
brenda
Schmiderer, C.; Grausgruber-Groeger, S.; Grassi, P.; Steinborn, R.; Novak, J.
Influence of gibberellin and daminozide on the expression of terpene synthases and on monoterpenes in common sage (Salvia officinalis)
J. Plant Physiol.
167
779-786
2010
Salvia officinalis (O81193)
brenda
Croteau, R.; Alonso, W.R.; Koepp, A.E.; Johnson, M.A.
Biosynthesis of monoterpenes: partial purification, characterization, and mechanism of action of 1,8-cineole synthase
Arch. Biochem. Biophys.
309
184-192
1994
Salvia officinalis (O81191), Salvia officinalis
brenda
Peters, R.J.; Croteau, R.B.
Alternative termination chemistries utilized by monoterpene cyclases: chimeric analysis of bornyl diphosphate, 1,8-cineole, and sabinene synthases
Arch. Biochem. Biophys.
417
203-211
2003
Salvia officinalis (O81191), Salvia officinalis
brenda
Wise, M.L.; Urbansky, M.; Helms, G.L.; Coates, R.M.; Croteau, R.
Syn stereochemistry of cyclic ether formation in 1,8-cineole biosynthesis catalyzed by recombinant synthase from Salvia officinalis
J. Am. Chem. Soc.
124
8546-8547
2002
Salvia officinalis (O81191), Salvia officinalis
brenda
Grausgruber-Groeger, S.; Schmiderer, C.; Steinborn, R.; Novak, J.
Seasonal influence on gene expression of monoterpene synthases in Salvia officinalis (Lamiaceae)
J. Plant Physiol.
169
353-359
2012
Salvia officinalis
brenda
Faehnrich, A.; Krause, K.; Piechulla, B.
Product variability of the cineole cassette monoterpene synthases of related Nicotiana species
Mol. Plant
4
965-984
2011
Nicotiana alata (H6WZF2), Nicotiana langsdorffii (H2ELN1)
brenda
Keszei, A.; Brubaker, C.L.; Carter, R.; Koellner, T.; Degenhardt, J.; Foley, W.J.
Functional and evolutionary relationships between terpene synthases from Australian Myrtaceae
Phytochemistry
71
844-852
2010
Eucalyptus sideroxylon
brenda
Kampranis, S.C.; Ioannidis, D.; Purvis, A.; Mahrez, W.; Ninga, E.; Katerelos, N.A.; Anssour, S.; Dunwell, J.M.; Degenhardt, J.; Makris, A.M.; Goodenough, P.W.; Johnson, C.B.
Rational conversion of substrate and product specificity in a Salvia monoterpene synthase: structural insights into the evolution of terpene synthase function
Plant Cell
19
1994-2005
2007
Salvia fruticosa (A6XH05), Salvia fruticosa
brenda
Roeder, S.; Hartmann, A.M.; Effmert, U.; Piechulla, B.
Regulation of simultaneous synthesis of floral scent terpenoids by the 1,8-cineole synthase of Nicotiana suaveolens
Plant Mol. Biol.
65
107-124
2007
Nicotiana suaveolens (A5Y5L5), Nicotiana suaveolens
brenda
Demissie, Z.A.; Cella, M.A.; Sarker, L.S.; Thompson, T.J.; Rheault, M.R.; Mahmoud, S.S.
Cloning, functional characterization and genomic organization of 1,8-cineole synthases from Lavandula
Plant Mol. Biol.
79
393-411
2012
Lavandula x intermedia (I3WEV8)
brenda
Chen, F.; Ro, D.K.; Petri, J.; Gershenzon, J.; Bohlmann, J.; Pichersky, E.; Tholl, D.
Characterization of a root-specific Arabidopsis terpene synthase responsible for the formation of the volatile monoterpene 1,8-cineole
Plant Physiol.
135
1956-1966
2004
Arabidopsis thaliana (P0DI76), Arabidopsis thaliana (P0DI77)
brenda
Nakano, C.; Kim, H.; Ohnishi, Y.
Identification of the first bacterial monoterpene cyclase, a 1,8-cineole synthase, that catalyzes the direct conversion of geranyl diphosphate
ChemBioChem
12
1988-1991
2011
Streptomyces clavuligerus (B5GMG2), Streptomyces clavuligerus DSM 738 (B5GMG2)
brenda
Faehnrich, A.; Brosemann, A.; Teske, L.; Neumann, M.; Piechulla, B.
Synthesis of cineole cassette monoterpenes in Nicotiana section Alatae: gene isolation, expression, functional characterization and phylogenetic analysis
Plant Mol. Biol.
79
537-553
2012
Nicotiana bonariensis (I7C6Y2), Nicotiana forgetiana (I7CTV3), Nicotiana longiflora (I7D3D7)
brenda
Faehnrich, A.; Neumann, M.; Piechulla, B.
Characteristic alatoid cineole cassette monoterpene synthase present in Nicotiana noctiflora
Plant Mol. Biol.
85
135-145
2014
Nicotiana noctiflora (W8GLB1)
brenda
Ruan, J.X.; Li, J.X.; Fang, X.; Wang, L.J.; Hu, W.L.; Chen, X.Y.; Yang, C.Q.
Isolation and characterization of three new monoterpene synthases from Artemisia annua
Front. Plant Sci.
7
638
2016
Artemisia annua (A0A068L889), Artemisia annua
brenda
Yahyaa, M.; Matsuba, Y.; Brandt, W.; Doron-Faigenboim, A.; Bar, E.; McClain, A.; Davidovich-Rikanati, R.; Lewinsohn, E.; Pichersky, E.; Ibdah, M.
Identification, functional characterization, and evolution of terpene synthases from a basal dicot
Plant Physiol.
169
1683-1697
2015
Laurus nobilis (A0A0H4U5M2)
brenda
Piechulla, B.; Bartelt, R.; Brosemann, A.; Effmert, U.; Bouwmeester, H.; Hippauf, F.; Brandt, W.
The alpha-terpineol to 1,8-cineole cyclization reaction of tobacco terpene synthases
Plant Physiol.
172
2120-2131
2016
Nicotiana suaveolens (A5Y5L5), Nicotiana forgetiana (I7CTV3)
brenda